Table 2. Data collection and refinement statistics.

		Crystals of HNP1 mutants
		I20A	I20A/L25A		Y16A/F28A		Y16A/I20A/L25A/F28A
Data collection
Wavelength, Å		1.54	1.54		0.98		1.00
Space group		P41	C2		H3		H3
Cell parameters
a, b, c, Å		37.7, 37.7, 40.5	75.0, 62.6, 42.5		88.6, 88.6, 54.1		83.8, 83.8, 51.3
α, β, γ, °		90, 90, 90	90, 99.7, 90		90, 90, 120		90, 90, 120
Molecules/a.u.		2	8		4		4
Resolution, (Å)a		50-1.7 (1.73-1.7)	50-1.66 (1.69-1.66)		50-2.0 (2.03-2.00)		50.0-1.9 (1.93-1.90)
# of reflections
Total		17,297	73,805		58,691		60,651
Unique		8,953	22,465		10,671		10,457
Rmerg b, %		13.9 (67.4)	8.1 (44.8)		10.3 (75.9)		3.6 (96.0)
I/σ		12.7 (2.0)	16.5 (1.6)		21.6 (1.3)		56 (2.2)
Completeness, %		100 (99.0)	98.3 (84.1)		99.5 (98.5)		99.1 (100)
Redundancy		4.8 (3.8)	2.3 (3.3)		5.5 (4.2)		5.8 (5.8)
Refinement Statistics
Resolution, Å	27.6-1.72			20-1.70		18.0-2.00		24.2-1.90
Rc, %	20.1			18.5		19.0		19.9
Rfree d, %	22.9			23.1		22.8		23.6
# of atoms
Protein	470			1,815		900		876
Water	26			209		8		8
Ligand/Ion	6			6		0		0
Overall B value (Å)2
Protein	38.2			28.6		64.8		72.7
Water	46.3			37.8		60.8		67.0
Ligand/Ion	67.6			20.9		–		–
Root mean square deviation
Bond lengths, Å	0.015			0.024		0.018		0.007
Bond angles,°	1.6			1.9		1.9		1.33
Ramachandrane
favored, %	94.6			96.8		96.4		94.4
allowed, %	5.4			3.2		3.6		3.6
outliers, %	0.0			0.0		0.0		0.0
PDB code	4LBB			4LBF		4LB1		4LB7

^aValues in parentheses are for highest-resolution shell.

^b R _merge = ∑|I - <I>|/∑I, where I is the observed intensity and <I> is the average intensity obtained from multiple observations of symmetry-related reflections after rejections.

^c R = ∑||F_o|- | F_c||/∑|F_o |, where F_o and F_c are the observed and calculated structure factors, respectively.

^dR_free = defined by by Brünger [68].

^eCalculated with MolProbity [48].